1z9s

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(New page: 200px<br /><applet load="1z9s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z9s, resolution 2.2&Aring;" /> '''Crystal Structure of ...)
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[[Image:1z9s.gif|left|200px]]<br /><applet load="1z9s" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1z9s, resolution 2.2&Aring;" />
 
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'''Crystal Structure of the native chaperone:subunit:subunit Caf1M:Caf1:Caf1 complex'''<br />
 
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==Overview==
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==Crystal Structure of the native chaperone:subunit:subunit Caf1M:Caf1:Caf1 complex==
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Periplasmic chaperone/usher machineries are used for assembly of, filamentous adhesion organelles of Gram-negative pathogens in a process, that has been suggested to be driven by folding energy. Structures of, mutant chaperone-subunit complexes revealed a final folding transition, (condensation of the subunit hydrophobic core) on the release of organelle, subunit from the chaperone-subunit pre-assembly complex and incorporation, into the final fibre structure. However, in view of the large interface, between chaperone and subunit in the pre-assembly complex and the reported, stability of this complex, it is difficult to understand how final folding, could release sufficient energy to drive assembly. In the present paper, we show the X-ray structure for a native chaperone-fibre complex that, together with thermodynamic data, shows that the final folding step is, indeed an essential component of the assembly process. We show that, completion of the hydrophobic core and incorporation into the fibre, results in an exceptionally stable module, whereas the chaperone-subunit, pre-assembly complex is greatly destabilized by the high-energy, conformation of the bound subunit. This difference in stabilities creates, a free energy potential that drives fibre formation.
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<StructureSection load='1z9s' size='340' side='right'caption='[[1z9s]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1z9s]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z9S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z9S FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z9s OCA], [https://pdbe.org/1z9s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z9s RCSB], [https://www.ebi.ac.uk/pdbsum/1z9s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z9s ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAF1M_YERPE CAF1M_YERPE] Has a stimulatory role for the envelope antigen F1 secretion. It seems to interact with the subunit polypeptide and to prevent it from digestion by a protease.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z9/1z9s_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1z9s ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Periplasmic chaperone/usher machineries are used for assembly of filamentous adhesion organelles of Gram-negative pathogens in a process that has been suggested to be driven by folding energy. Structures of mutant chaperone-subunit complexes revealed a final folding transition (condensation of the subunit hydrophobic core) on the release of organelle subunit from the chaperone-subunit pre-assembly complex and incorporation into the final fibre structure. However, in view of the large interface between chaperone and subunit in the pre-assembly complex and the reported stability of this complex, it is difficult to understand how final folding could release sufficient energy to drive assembly. In the present paper, we show the X-ray structure for a native chaperone-fibre complex that, together with thermodynamic data, shows that the final folding step is indeed an essential component of the assembly process. We show that completion of the hydrophobic core and incorporation into the fibre results in an exceptionally stable module, whereas the chaperone-subunit pre-assembly complex is greatly destabilized by the high-energy conformation of the bound subunit. This difference in stabilities creates a free energy potential that drives fibre formation.
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==About this Structure==
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Resolving the energy paradox of chaperone/usher-mediated fibre assembly.,Zavialov AV, Tischenko VM, Fooks LJ, Brandsdal BO, Aqvist J, Zav'yalov VP, Macintyre S, Knight SD Biochem J. 2005 Aug 1;389(Pt 3):685-94. PMID:15799718<ref>PMID:15799718</ref>
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1Z9S is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z9S OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Resolving the energy paradox of chaperone/usher-mediated fibre assembly., Zavialov AV, Tischenko VM, Fooks LJ, Brandsdal BO, Aqvist J, Zav'yalov VP, Macintyre S, Knight SD, Biochem J. 2005 Aug 1;389(Pt 3):685-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15799718 15799718]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 1z9s" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Yersinia pestis]]
[[Category: Yersinia pestis]]
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[[Category: Aqvist, J.]]
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[[Category: Aqvist J]]
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[[Category: Brandsdal, B.O.]]
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[[Category: Brandsdal BO]]
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[[Category: Fooks, L.J.]]
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[[Category: Fooks LJ]]
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[[Category: Knight, S.D.]]
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[[Category: Knight SD]]
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[[Category: Macintyre, S.]]
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[[Category: Macintyre S]]
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[[Category: Tischenko, V.M.]]
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[[Category: Tischenko VM]]
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[[Category: Zavialov, A.V.]]
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[[Category: Zav'yalov VP]]
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[[Category: yalov, V.P.Zav.]]
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[[Category: Zavialov AV]]
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[[Category: chaperone-usher pathway]]
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[[Category: donor strand complementation]]
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[[Category: native minimal fiber]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:19:49 2007''
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Current revision

Crystal Structure of the native chaperone:subunit:subunit Caf1M:Caf1:Caf1 complex

PDB ID 1z9s

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